DNA-directed DNA polymerase - P00581 (DPOL_BPT7)

Protein Feature View of PDB entries mapped to a UniProtKB sequence

Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.
UniProt

Composed of two subunits. One is encoded by the phage and the other is encoded by the host thioredoxin. Interacts with helicase/primase gp4; this interaction is essential for the coordination of DNA unwinding and nucleotide polymerization on duplex DNA. Interacts with the ssDNA-binding protein gp2.5.
UniProt

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Validation Track